EC Number   |
Application |
Reference |
|---|
   3.4.24.13 | medicine |
bacterial IgA proteases are potential candidates as vaccine |
37011 |
| 3.4.24.13 | medicine |
enzyme is a major Streptococcus pneumoniae antigen in humans |
666834 |
| 3.4.24.13 | medicine |
enzyme, as well as pneumococcal proteins alpha-enolase, immunoglobulin streptococcal lipoprotein rotamase A, and putative proteinase maturation protein A are immunogenic proteins that elicit antibody response early in life. No significant correlation between antibody titers to these proteins and pneumococcal carriage or infection |
670985 |
| 3.4.24.13 | medicine |
IgA1 protease is a surface protective antigen of Streptococcus suis serotype 2 (SS2), immunization with purified recombinant IgA1 protease (amino acid residues 600-1926) induces high IgG antibody titers and confers complete protection against a challenge with a lethal dose of SS2 in a mouse model. rIgAP emulsified with a Marcol 52-based adjuvant can induce high titers of specific IgG antibodies, including high levels of antibodies with bactericidal activity in the presence of phagocytes, as well as confer good protection against SS2 infection. The virulence-associated protein IgA1 protease is a protective antigen and one of promising and effective vaccine candidates against SS2 |
-, 754643 |
| 3.4.24.13 | medicine |
IgA1 protease may be an effective therapeutic candidate for IgAN by removing the mesangial deposited IgA1 in glomerular mesangium leading to immunoglobulin A nephropathy. The removal of IgA1 by IgA1 protease may separate the IgA1-containing immune complexes thereby eliminating its other components at the same time |
718166 |
| 3.4.24.13 | medicine |
immunization of animals with IgA1pr MA28-P1004LEH6 or proteins I, II, III provides the formation of immunological memory and can protect against both meningococcal and a number of pneumococcal fatal infections. Protective properties of meningococcal IgA1pr MA28-P1004LEH6 and proteins I, II, III against pneumococci may be attributed to their conformational epitopes close in structure to epitopes of pneumococcal surface proteins. In the model of passive animal protection, sera from rabbits immunized with Streptococcus pneumoniae of different serotypes are shown to be capable of animal protection from infection with Neisseria meningitidis, at least serogroup B. Pneumococcal and meningococcal infections can cause a crossprotective effect. This makes meningococcal IgA1 proteases and their recombinant derivatives the potential components of polyvalent vaccines |
-, 754644 |
| 3.4.24.13 | medicine |
systemically administered IgA protease is able to remove glomerular IgA immune complexes, both the antigen and antibody components, in a passive mouse model of IgA nephropathy. IgA protease decreases the amount of injected human IgA immune complexes deposited in the kidneys in vivo. The quantity of deposited complexes is reduced by digestion of IgA1 at a single site, the peptide bond between amino acid residues 231-232 in each alpha chain |
695450 |
| 3.4.24.13 | medicine |
the broad and specific recognition of the epiA polypeptide by human sera demonstrate that the pneumococcal IgA1 protease contains an immunodominant B-cell epitope |
678940 |
| 3.4.24.13 | medicine |
three of the igA gene restriction types, which appear to represent 98% of the Haemophilus influenzae serotype b population, encode IgA1 proteases that are inhibited by antisera to any one of theses types and therefore could form the basis for the development of a vaccine against Haemophilus influenzae meningitis |
37031 |
